IPB2_YEAST
ID IPB2_YEAST Reviewed; 75 AA.
AC P0CT04; D6W1G3; P01095;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Protease B inhibitor 2;
DE AltName: Full=Proteinase inhibitor I(B)2;
GN Name=PBI2; OrderedLocusNames=YNL015W; ORFNames=N2844;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP PROTEIN SEQUENCE OF 2-75, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=387783; DOI=10.1016/s0021-9258(19)86350-0;
RA Maier K., Mueller H., Tesch R., Trolp R., Witt I., Holzer H.;
RT "Primary structure of yeast proteinase B inhibitor 2.";
RL J. Biol. Chem. 254:12555-12561(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2015812; DOI=10.1111/j.1432-1033.1991.tb15874.x;
RA Schu P., Wolf D.H.;
RT "The proteinase yscB inhibitor (PBI2) gene of yeast and studies on the
RT function of its protein product.";
RL Eur. J. Biochem. 197:1-7(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (INHIBITOR 2).
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP PROTEIN SEQUENCE OF 42-54, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K91-1A;
RX PubMed=9159115; DOI=10.1073/pnas.94.11.5582;
RA Slusarewicz P., Xu Z., Seefeld K., Haas A., Wickner W.T.;
RT "I2B is a small cytosolic protein that participates in vacuole fusion.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5582-5587(1997).
RN [7]
RP ORIGIN OF SEQUENCE, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 26109 / X2180 / NCYC 826;
RX PubMed=1100120; DOI=10.1016/0304-4165(75)90155-5;
RA Betz H.;
RT "Levels and turnover of the proteinase B inhibitors in yeast.";
RL Biochim. Biophys. Acta 404:142-151(1975).
RN [8]
RP ORIGIN OF SEQUENCE.
RC STRAIN=ATCC 26109 / X2180 / NCYC 826;
RX PubMed=328499; DOI=10.1016/s0021-9258(19)63349-1;
RA Buenning P., Holzer H.;
RT "Natural occurrence and chemical modification of proteinase B inhibitors
RT from yeast.";
RL J. Biol. Chem. 252:5316-5323(1977).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN THE LMA1 COMPLEX.
RX PubMed=9015301; DOI=10.1083/jcb.136.2.299;
RA Xu Z., Mayer A., Muller E.G.D., Wickner W.;
RT "A heterodimer of thioredoxin and I(B)2 cooperates with Sec18p (NSF) to
RT promote yeast vacuole inheritance.";
RL J. Cell Biol. 136:299-306(1997).
RN [10]
RP FUNCTION, AND INTERACTION OF THE LMA1 COMPLEX WITH SEC18.
RX PubMed=9657146; DOI=10.1016/s0092-8674(00)81457-9;
RA Xu Z., Sato K., Wickner W.;
RT "LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a
RT t-SNARE (Vam3p) complex, and is released during fusion.";
RL Cell 93:1125-1134(1998).
RN [11]
RP REVIEW, AND FUNCTION OF THE LMA1 COMPLEX IN VESICLE FUSION.
RX PubMed=12914955; DOI=10.1016/s0167-4889(03)00086-7;
RA Elazar Z., Scherz-Shouval R., Shorer H.;
RT "Involvement of LMA1 and GATE-16 family members in intracellular membrane
RT dynamics.";
RL Biochim. Biophys. Acta 1641:145-156(2003).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Cytosolic inhibitor of vacuolar proteinase B (yscB), probably
CC regulating protease B activity during limited proteolysis. PBI2 is a
CC component of the LMA1 complex, which is involved in the facilitation of
CC vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle
CC fusion with the Golgi. {ECO:0000269|PubMed:12914955,
CC ECO:0000269|PubMed:2015812, ECO:0000269|PubMed:9015301,
CC ECO:0000269|PubMed:9159115, ECO:0000269|PubMed:9657146}.
CC -!- SUBUNIT: Part of the heterodimeric LMA1 complex together with the
CC thioredoxin II/TRX2. LMA1 binds to the ATPase SEC18.
CC {ECO:0000269|PubMed:9015301, ECO:0000269|PubMed:9657146}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1100120,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9159115}.
CC -!- MISCELLANEOUS: Originally, 2 inhibitors of protease B, inhibitor I(B)2
CC and inhibitor I(B)1, have been isolated from commercial baker's yeast,
CC which consists of both S.cerevisiae and S.carlsbergensis. It has been
CC shown that S.cerevisiae only produces inhibitor 2, and S.carlsbergensis
CC only produces inhibitor 1 (PubMed:328499). A sequence for inhibitor 1
CC from S.carlsbergensis has been determined (AC P0CT05).
CC {ECO:0000305|PubMed:328499}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I9 family. {ECO:0000305}.
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DR EMBL; X60051; CAA42651.1; -; Genomic_DNA.
DR EMBL; Z71291; CAA95876.1; -; Genomic_DNA.
DR EMBL; AY693217; AAT93236.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10529.1; -; Genomic_DNA.
DR PIR; S16882; YBBY2.
DR RefSeq; NP_014383.1; NM_001182854.1.
DR AlphaFoldDB; P0CT04; -.
DR SMR; P0CT04; -.
DR BioGRID; 35811; 76.
DR ComplexPortal; CPX-1278; LMA1 complex, TRX1 variant.
DR ComplexPortal; CPX-1279; LMA1 complex, TRX2 variant.
DR IntAct; P0CT04; 4.
DR STRING; 4932.YNL015W; -.
DR MEROPS; I09.003; -.
DR iPTMnet; P0CT04; -.
DR PaxDb; P0CT04; -.
DR PRIDE; P0CT04; -.
DR EnsemblFungi; YNL015W_mRNA; YNL015W; YNL015W.
DR GeneID; 855717; -.
DR KEGG; sce:YNL015W; -.
DR SGD; S000004960; PBI2.
DR VEuPathDB; FungiDB:YNL015W; -.
DR eggNOG; ENOG502SBW1; Eukaryota.
DR HOGENOM; CLU_156026_3_0_1; -.
DR OMA; DKEVHAN; -.
DR BioCyc; YEAST:MON3O-39566; -.
DR PRO; PR:P0CT04; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P0CT04; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; IC:ComplexPortal.
DR GO; GO:0120124; C:membrane fusion priming complex; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:SGD.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0030162; P:regulation of proteolysis; IMP:SGD.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IDA:SGD.
DR Gene3D; 3.30.70.80; -; 1.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Phosphoprotein; Protease inhibitor;
KW Protein transport; Reference proteome; Serine protease inhibitor;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:387783"
FT CHAIN 2..75
FT /note="Protease B inhibitor 2"
FT /id="PRO_0000212790"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 33
FT /note="V -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 75 AA; 8590 MW; 5C39E20240A4C8A8 CRC64;
MTKNFIVTLK KNTPDVEAKK FLDSVHHAGG SIVHEFDIIK GYTIKVPDVL HLNKLKEKHN
DVIENVEEDK EVHTN
